ArticleMethods in enzymology2013
Expression of mammalian G protein-coupled receptors in Caenorhabditis elegans.
Article in Methods in enzymology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Apo-Opsin Exists in Equilibrium Between a Predominant Inactive and a Rare Highly Active State.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Inherent instability of the retinitis pigmentosa P23H mutant opsin.The Journal of biological chemistry · 2014Article
- Autosomal recessive retinitis pigmentosa E150K opsin mice exhibit photoreceptor disorganization.The Journal of clinical investigation · 2013Article
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Authors and funding
7 authors.
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Abstract
Constituting the largest group of membrane proteins identified in the human genome, G protein-coupled receptors (GPCRs) help control many physiological processes by responding to various stimuli. As targets for more than 40% of all prescribed pharmaceuticals, detailed understanding of GPCR structures is vital for the design and development of more specific medications and improved patient therapies. But structural information for membrane proteins and GPCRs, in particular, is limited despite considerable interest. The major impediment to obtaining sufficient quantities of highly purified GPCRs in their native form for crystallization lies in their low tissue levels, poor yields, and stability. The only exception is rhodopsin, which is abundantly expressed in the eye and stabilized by its covalently bound chromophore, 11-cis-retinal. Expression systems and purification protocols have yet to be developed for all other GPCRs. Here, we present a novel expression system for human GPCRs in Caenorhabditis elegans that produces sufficient amounts of recombinant proteins to allow their biochemical and structural characterization.
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